Structure of mouse L-chain ferritin at 1.6 Å resolution

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 57; no. 11; pp. 1491 - 1497
• Main Authors: Granier, Thierry, Gallois, Bernard, Langlois d'Estaintot, Béatrice, Dautant, Alain, Chevalier, Jean-Marc, Mellado, Jean-Marc, Beaumont, Carole, Santambrogio, Paolo, Arosio, Paolo, Precigoux, Gilles
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-11-2001
• Subjects: Animals; Binding Sites; Crystallization; Crystallography, X-Ray; Ferritins - chemistry; Hydrogen Bonding; L-chain ferritin; Metals - metabolism; Mice; Models, Molecular; Protein Conformation; Recombinant Proteins - chemistry; Salts - chemistry; Temperature
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444901008897

Cubic F432 crystals of recombinant mouse L‐chain apoferritin were obtained by the hanging‐drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 Å resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight‐amino‐acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature.